PAGP_LEGP2
ID PAGP_LEGP2 Reviewed; 190 AA.
AC D5T5P7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000255|HAMAP-Rule:MF_00837};
DE EC=2.3.1.251 {ECO:0000255|HAMAP-Rule:MF_00837};
DE AltName: Full=Lipid A acylation protein {ECO:0000255|HAMAP-Rule:MF_00837};
DE Flags: Precursor;
GN Name=pagP {ECO:0000255|HAMAP-Rule:MF_00837}; OrderedLocusNames=lpa_00034;
OS Legionella pneumophila serogroup 1 (strain 2300/99 Alcoy).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=423212;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2300/99 Alcoy;
RX PubMed=20236513; DOI=10.1186/1471-2164-11-181;
RA D'Auria G., Jimenez-Hernandez N., Peris-Bondia F., Moya A., Latorre A.;
RT "Legionella pneumophila pangenome reveals strain-specific virulence
RT factors.";
RL BMC Genomics 11:181-181(2010).
CC -!- FUNCTION: Transfers a palmitate residue from the sn-1 position of a
CC phospholipid to the N-linked hydroxymyristate on the proximal unit of
CC lipid A or its precursors. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid A
CC (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid
CC A; Xref=Rhea:RHEA:46864, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369,
CC ChEBI:CHEBI:87048, ChEBI:CHEBI:134257; EC=2.3.1.251;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA
CC = a 2-acyl-sn-glycero-3-phosphocholine + lipid IIB;
CC Xref=Rhea:RHEA:46872, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369,
CC ChEBI:CHEBI:86226, ChEBI:CHEBI:87058; EC=2.3.1.251;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA
CC (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + lipid IVB;
CC Xref=Rhea:RHEA:46868, ChEBI:CHEBI:57875, ChEBI:CHEBI:58603,
CC ChEBI:CHEBI:77369, ChEBI:CHEBI:87049; EC=2.3.1.251;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00837}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001828; ADG23271.1; -; Genomic_DNA.
DR RefSeq; WP_013100946.1; NC_014125.1.
DR AlphaFoldDB; D5T5P7; -.
DR SMR; D5T5P7; -.
DR KEGG; lpa:lpa_00034; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; DSHNEWQ; -.
DR BioCyc; LPNE423212:LPA_RS00125-MON; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00837; PagP_transferase; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR009746; Peptid-resist/lipidA_acyl_PagP.
DR Pfam; PF07017; PagP; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell outer membrane; Membrane; Signal; Transferase.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 19..190
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414462"
FT ACT_SITE 60
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 69
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 190 AA; 21187 MW; 4DE12EA2EBB1DDA8 CRC64;
MKRLISCLTI ICALNASAAA ETTSNPCSRW ISFLKPVCQR IHQTWAEGHD DMYFSGYAWH
NRYVYSNEKI KSYNETAWGG GLGKSLFDEK GNWHGLYAIA FLDSHRHLEP AVGYAYLKTA
SVNKDLKAGL GYSVLVTSRV DYDNVPIPGA LPWAALFYKR ITIAATYIPG SSREGHENGN
VLYMLGKISL